8T6R
Acinetobacter baumannii 118362 family 2A cargo-loaded encapsulin shell
Summary for 8T6R
| Entry DOI | 10.2210/pdb8t6r/pdb |
| EMDB information | 41078 |
| Descriptor | Major membrane protein I (1 entity in total) |
| Functional Keywords | encapsulin, virus like particle, protein nanocompartment |
| Biological source | Acinetobacter baumannii 118362 |
| Total number of polymer chains | 1 |
| Total formula weight | 34609.19 |
| Authors | |
| Primary citation | Benisch, R.,Andreas, M.P.,Giessen, T.W. A widespread bacterial protein compartment sequesters and stores elemental sulfur. Sci Adv, 10:eadk9345-eadk9345, 2024 Cited by PubMed Abstract: Subcellular compartments often serve to store nutrients or sequester labile or toxic compounds. As bacteria mostly do not possess membrane-bound organelles, they often have to rely on protein-based compartments. Encapsulins are one of the most prevalent protein-based compartmentalization strategies found in prokaryotes. Here, we show that desulfurase encapsulins can sequester and store large amounts of crystalline elemental sulfur. We determine the 1.78-angstrom cryo-EM structure of a 24-nanometer desulfurase-loaded encapsulin. Elemental sulfur crystals can be formed inside the encapsulin shell in a desulfurase-dependent manner with l-cysteine as the sulfur donor. Sulfur accumulation can be influenced by the concentration and type of sulfur source in growth medium. The selectively permeable protein shell allows the storage of redox-labile elemental sulfur by excluding cellular reducing agents, while encapsulation substantially improves desulfurase activity and stability. These findings represent an example of a protein compartment able to accumulate and store elemental sulfur. PubMed: 38306423DOI: 10.1126/sciadv.adk9345 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.78 Å) |
Structure validation
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